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Database: UniProt
Entry: G1QGF0_MYOLU
LinkDB: G1QGF0_MYOLU
Original site: G1QGF0_MYOLU 
ID   G1QGF0_MYOLU            Unreviewed;       529 AA.
AC   G1QGF0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 3 {ECO:0000313|Ensembl:ENSMLUP00000022783.1};
GN   Name=ENTPD3 {ECO:0000313|Ensembl:ENSMLUP00000022783.1};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000022783.1, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000022783.1, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000022783.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR   EMBL; AAPE02039235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02039236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1QGF0; -.
DR   STRING; 59463.ENSMLUP00000022783; -.
DR   Ensembl; ENSMLUT00000023063.1; ENSMLUP00000022783.1; ENSMLUG00000028733.1.
DR   eggNOG; KOG1386; Eukaryota.
DR   GeneTree; ENSGT01100000263542; -.
DR   HOGENOM; CLU_010246_2_3_1; -.
DR   InParanoid; G1QGF0; -.
DR   OMA; GNAISDM; -.
DR   TreeFam; TF332859; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:Ensembl.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:Ensembl.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IEA:Ensembl.
DR   GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:Ensembl.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF38; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 3; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU003833};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        487..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         222..226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   529 AA;  59053 MW;  C60213F2149FC10E CRC64;
     MLTVLTRQPC EHAGFKALSR TPVVVALVVL ILSVVVLVAI TLIQIHQKEV LLPGLKYGIV
     LDAGSSRTTV YVYQWPAEKE NNTGVVTQTS RCSVKGSGIS SYGKNPQDAP KAFEDCMRKV
     KEQIPAHLQG STHIYLGATA GMRLLRLQNE TAANEVLASI QNYFKSQPFD FRGAQIISGQ
     EEGIYGWITA NYLMGNFLEK DLWHMWVHPN GVETTGALDL GGASTQISFA VGEKAELNTS
     DIIKVSLYGY VYTLYTRSFQ CYGRNEAEKR FLAMLLQVPE NDSSPGIPCY PRNYSTTFTA
     GHLFDSLCTE ELRPGGYDPD DTITFEGTGD PLLCRVKVAS LFAFRACHDR EICCFDGVYQ
     PEVKGSFVAF AGFFYTANAL NLSGSFSLNA FNSSTWDFCS QDWSQLPLLL PRFDEVYARS
     YCFSAHYIYH LLVSGYKFTE DTWPQIHFKK EVDNSSIAWS LGYMLTLTNQ IPAEIPLIRL
     PMKPPTFMSV LAFFTGVALL CLGFLVYLYA LSRNQRRSQH ALDHAVDSE
//
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